6LTW

Crystal structure of Apo form of I122A/I330A variant of S-adenosylmethionine synthetase from Cryptosporidium hominis

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d6ltwa1	Alpha and beta proteins (a+b)	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	automated matches	automated matches	(Cryptosporidium hominis ) [TaxId: 237895 ],	SCOPe (2.08)
B	d6ltwb1	Alpha and beta proteins (a+b)	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	automated matches	automated matches	(Cryptosporidium hominis ) [TaxId: 237895 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	S-AdoMet_synt_C	e6ltwA3	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_C	ECOD (1.6)
A	S-AdoMet_synt_M	e6ltwA2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_M	ECOD (1.6)
A	S-AdoMet_synt_N	e6ltwA1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_N	ECOD (1.6)
B	S-AdoMet_synt_C	e6ltwB3	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_C	ECOD (1.6)
B	S-AdoMet_synt_M	e6ltwB2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_M	ECOD (1.6)
B	S-AdoMet_synt_N	e6ltwB1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_N	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00438	S-adenosylmethionine synthetase, N-terminal domain (S-AdoMet_synt_N)	S-adenosylmethionine synthetase, N-terminal domain	The three domains of S-adenosylmethionine synthetase have the same alpha+beta fold.	Domain
A, B	PF02773	S-adenosylmethionine synthetase, C-terminal domain (S-AdoMet_synt_C)	S-adenosylmethionine synthetase, C-terminal domain	The three domains of S-adenosylmethionine synthetase have the same alpha+beta fold.	Domain
A, B	PF02772	S-adenosylmethionine synthetase, central domain (S-AdoMet_synt_M)	S-adenosylmethionine synthetase, central domain	The three domains of S-adenosylmethionine synthetase have the same alpha+beta fold.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	S-adenosylmethionine synthase	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding methionine adenosyltransferase activity transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups catalytic activity cation binding metal ion binding	sulfur compound biosynthetic process biosynthetic process S-adenosylmethionine biosynthetic process cellular biosynthetic process cellular metabolic process S-adenosylmethionine metabolic process sulfur compound metabolic process metabolic process cellular process small molecule metabolic process one-carbon metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR022631	S-adenosylmethionine synthetase, conserved site	Conserved Site
A, B	IPR022630	S-adenosylmethionine synthetase, C-terminal	Domain
A, B	IPR002133	S-adenosylmethionine synthetase	Family
A, B	IPR022636	S-adenosylmethionine synthetase superfamily	Homologous Superfamily
A, B	IPR022629	S-adenosylmethionine synthetase, central domain	Domain
A, B	IPR022628	S-adenosylmethionine synthetase, N-terminal	Domain

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.